› 6z7h

X-ray diffraction
1.42Å resolution

Structure of CTX-M-15 E166Q mutant crystallised in the presence of enmetazobactam (AAI101)

Released:
DOI: 10.2210/pdb6z7h/pdb
Model geometry
Fit model/data
PDB entry 6z7h coloured by chain, front view.
PDB entry 6z7h coloured by chain, side view.
PDB entry 6z7h coloured by chain, top view.
Source organism: Klebsiella pneumoniae IS53
Primary publication:
Penicillanic Acid Sulfones Inactivate the Extended-Spectrum β-Lactamase CTX-M-15 through Formation of a Serine-Lysine Cross-Link: an Alternative Mechanism of β-Lactamase Inhibition.
Hinchliffe P, Tooke CL, Bethel CR, Wang B, Arthur C, Heesom KJ, Shapiro S, Schlatzer DM, Papp-Wallace KM, Bonomo RA, Spencer J
OpenAccess logo mBio 13 e0179321 (2022)
PMID: 35612361

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-237369 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 28.28 KDa
Source organism: Klebsiella pneumoniae IS53
Expression system: Escherichia coli

Ligands and Environments

3 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
Ligand CL 1 x CL
1 modified residue:
Ligand DAL 1 x DAL

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 44.935Å b: 45.898Å c: 118.212Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.138 0.173
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Biochemical exploration of β-lactamase inhibitors.
Arer et al. (2022)
1 other article

1 mention without citation

Penicillanic Acid Sulfones Inactivate the Extended-Spectrum β-Lactamase CTX-M-15 through Formation of a Serine-Lysine Cross-Link: an Alternative Mechanism of β-Lactamase Inhibition.
Hinchliffe et al. (2022)